ID A0A0M2NHQ1_9FIRM Unreviewed; 470 AA.
AC A0A0M2NHQ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN ORFNames=CHK_2578 {ECO:0000313|EMBL:KKI49962.1};
OS Christensenella hongkongensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC Christensenella.
OX NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI49962.1, ECO:0000313|Proteomes:UP000034076};
RN [1] {ECO:0000313|EMBL:KKI49962.1, ECO:0000313|Proteomes:UP000034076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU16 {ECO:0000313|EMBL:KKI49962.1,
RC ECO:0000313|Proteomes:UP000034076};
RA Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT "Draft genome sequence of bacteremic isolate Catabacter hongkongensis type
RT strain HKU16T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001240,
CC ECO:0000256|RuleBase:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000256|RuleBase:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKI49962.1}.
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DR EMBL; LAYJ01000115; KKI49962.1; -; Genomic_DNA.
DR RefSeq; WP_046444390.1; NZ_SMCZ01000009.1.
DR AlphaFoldDB; A0A0M2NHQ1; -.
DR STRING; 270498.CHK_2578; -.
DR PATRIC; fig|270498.16.peg.1323; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000034076; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01570; NAPRTase_A; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17956; NAPRTase_C; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:KKI49962.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Reference proteome {ECO:0000313|Proteomes:UP000034076};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:KKI49962.1}.
FT DOMAIN 1..125
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 147..335
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 353..462
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 470 AA; 52899 MW; FF4B81847B7A9CF1 CRC64;
MLTDLYQLTM MYGYYKAGKH NDTAVYDLFF RRQGDETNYA VCAGLEQVID LINNLRFEED
DIKYLRSLGL FDEEFMDYLR ELRFTGEIYA IPEGTVVFPM EPLVRVSAPI SQAQLIETAL
LNMVNHQTLI ATKASRVVYA AQGDAVLEFG LRRAQGPDAG IYGARAALIG GCTSTSNVLT
AQMFGATAAG THAHSWVMSF PDELTAFRAY AQTFPSGCML LVDTYDTLKS GIPNAITVFK
ELREKGYEPV GIRLDSGDLA YLSKRARKML DDAGFQNARI FASSDLDEYT IADLKQQGAK
IDVWGVGTRL ITGHDHPALG GVYKLSANIV DGEMIPKLKI SENVWKITNP GIKKIKRIYS
KADGMAIADL IMLESEEIDA NLPLTIFDPI ETWKKMTIVD YELRDLLVPV FVDGKQVYES
PCLKDIQEYA RKDMATFWDE FRRIKRPHLY KVDLSDGLYN LKKKLLNEKK
//